Calpains, Mitochondria and Apoptosis.

Cardiovasc Res. 2012 May 11;
Smith MA, Schnellmann RG

Mitochondrial activity is critical for efficient function of the cardiovascular system. In response to cardiovascular injury, mitochondrial dysfunction occurs and can lead to apoptosis and necrosis. Calpains are a 15 member family of Ca(2+)-activated cysteine proteases localized to the cytosol and mitochondria, and several have been shown to regulate apoptosis and necrosis. For example, in endothelial cells Ca(2+)-overload causes mitochondrial calpain 1 cleavage of the Na(+)/Ca(2+) exchanger leading to mitochondrial Ca(2+) accumulation. Also, activated calpain 1 cleaves Bid, inducing cytochrome c release and apoptosis. In renal cells, calpains 1 and 2 promote apoptosis and necrosis by cleaving cytoskeletal proteins, which increases plasma membrane permeability, and cleavage of caspases. Calpain 10 cleaves electron transport chain proteins, causing decreased mitochondrial respiration and excessive activation or inhibition of calpain 10 activity induces mitochondrial dysfunction and apoptosis. In cardiomyocytes, calpain 1 activates caspase 3 and poly ADP ribose polymerase during tumor necrosis factor-α-induced apoptosis and calpain 1 cleaves apoptosis inducing factor after Ca(2+) overload. Many of these observations have been elucidated with calpain inhibitors, but most calpain inhibitors are not specific for calpains or a specific calpain family member, creating more questions. The following review will discuss how calpains affect mitochondrial function and apoptosis within the cardiovascular system.

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Calpains, Mitochondria and Apoptosis.

A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein.

Dalton Trans. 2012 May 14;
Hongoh M, Haratake M, Fuchigami T, Nakayama M

In this paper, we describe a thiol-mediated and energy-dependent membrane transport of selenium by erythroid anion exchanger 1 (AE1, also known as band 3 protein). The AE1 is the most abundant integral protein of red cell membranes and plays a critical role in the carbon dioxide transport system in which carbon dioxide is carried as bicarbonate in the plasma. This protein mediates the membrane transport of selenium, an essential antioxidant micronutrient, from red cells to the plasma in a manner that is distinct from the already known anion exchange mechanism. In this pathway, selenium bound to the cysteine 93 of the hemoglobin β chain (Hb-Cysβ93) is transported by the relay mechanism to the Cys317 of the amino-terminal cytoplasmic domain of the AE1 on the basis of the intrinsic interaction between the two proteins and is subsequently exported to the plasma via the Cys843 of the membrane-spanning domain. The selenium export did not occur in plain isotonic buffer solutions and required thiols, such as albumin, in the outer medium. Such a membrane transport mechanism would also participate in the export pathways of the nitric oxide vasodilator activity and other thiol-reactive substances bound to the Hb-Cysβ93 from red cells to the plasma and/or peripherals.

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A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein.

A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein.

Dalton Trans. 2012 May 14;
Hongoh M, Haratake M, Fuchigami T, Nakayama M

In this paper, we describe a thiol-mediated and energy-dependent membrane transport of selenium by erythroid anion exchanger 1 (AE1, also known as band 3 protein). The AE1 is the most abundant integral protein of red cell membranes and plays a critical role in the carbon dioxide transport system in which carbon dioxide is carried as bicarbonate in the plasma. This protein mediates the membrane transport of selenium, an essential antioxidant micronutrient, from red cells to the plasma in a manner that is distinct from the already known anion exchange mechanism. In this pathway, selenium bound to the cysteine 93 of the hemoglobin β chain (Hb-Cysβ93) is transported by the relay mechanism to the Cys317 of the amino-terminal cytoplasmic domain of the AE1 on the basis of the intrinsic interaction between the two proteins and is subsequently exported to the plasma via the Cys843 of the membrane-spanning domain. The selenium export did not occur in plain isotonic buffer solutions and required thiols, such as albumin, in the outer medium. Such a membrane transport mechanism would also participate in the export pathways of the nitric oxide vasodilator activity and other thiol-reactive substances bound to the Hb-Cysβ93 from red cells to the plasma and/or peripherals.

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A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein.

Membrane Protein Transport, Volume 1: This is the first volume in a series on membrane protein transfer. Membran… http://t.co/92YcsM23

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Membrane Protein Transport, Volume 1: This is the first volume in a series on membrane protein transfer. Membran… http://t.co/92YcsM23

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Carrier protein – it has a receptor site that carries molecules through the plasma membrane by active transport of facilitated diffusion.

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the RhD protein is just a membrane transport protein has nothing to do with why (@YouTube http://t.co/SYDSmgeL)

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Membrane Protein Transport, Volume 1: This is the first volume in a series on membrane protein transfer. Membran… http://t.co/pE9pDfUo

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Photo: Ca2+ ATPase › Ca2+ ATPase is a protein which enables active transport of Ca2+ across the membrane of… http://t.co/Gsi1uw1y

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Facilitated difussion is a process of passive transport. aided by integral membrane proteins such as CARRIER protein and PORE protein

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Sequencing and analysis of four BAC clones containing innate immune genes from the Zhikong scallop (Chlamys farreri).

Gene. 2012 Apr 20;
Zhao C, Zhang T, Zhang X, Hu S, Xiang J

The sequencing of BAC clones (~100kb) can reveal some characteristics of a genome that are challenging to obtain based on short sequences. Additionally, although the immune genes of the Zhikong scallop (Chlamys farreri) have been studied widely, few analyses have been conducted at the DNA level. In this study, four C. farreri BAC clones containing innate immune genes, including hsp70, lgbp (lipopolysaccharide and beta-1,3-glucan binding protein), serine protease and a gene with an immunoglobulin-like domain, were sequenced and analyzed both to explore the genomic characteristics of C. farreri based on long DNA sequences and to promote the study of C. farreri immune genes at the DNA level. The total length of the four BACs was 389.98kb. A total of 34 genes were predicted in these sequences, and several features of protein-coding regions in the C. farreri genome were inferred based on this information. Two LGBP genes were located close to a 22-kb region in one BAC clone, indicating the physical linkage of some immune genes in C. farreri. A cluster of membrane transport genes was also observed; these genes might play important roles in eliminating toxins in C. farreri, which lives as a filter feeder. Further analysis showed 15.43% of the BAC sequence was repetitive. Tandem repeats were the most abundant repeat type, followed by transposable elements. A total of 31 SSRs were predicted in the four BACs. An IS10 family transposon was identified, and a suspected regulatory non-coding RNA gene for this transposon (RNA-OUT) was observed to overlap with it complementarily. This work will promote future studies on the genomics, immune system and non-coding regions of C. farreri.

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Sequencing and analysis of four BAC clones containing innate immune genes from the Zhikong scallop (Chlamys farreri).

Sequencing and analysis of four BAC clones containing innate immune genes from the Zhikong scallop (Chlamys farreri).

Gene. 2012 Apr 20;
Zhao C, Zhang T, Zhang X, Hu S, Xiang J

The sequencing of BAC clones (~100kb) can reveal some characteristics of a genome that are challenging to obtain based on short sequences. Additionally, although the immune genes of the Zhikong scallop (Chlamys farreri) have been studied widely, few analyses have been conducted at the DNA level. In this study, four C. farreri BAC clones containing innate immune genes, including hsp70, lgbp (lipopolysaccharide and beta-1,3-glucan binding protein), serine protease and a gene with an immunoglobulin-like domain, were sequenced and analyzed both to explore the genomic characteristics of C. farreri based on long DNA sequences and to promote the study of C. farreri immune genes at the DNA level. The total length of the four BACs was 389.98kb. A total of 34 genes were predicted in these sequences, and several features of protein-coding regions in the C. farreri genome were inferred based on this information. Two LGBP genes were located close to a 22-kb region in one BAC clone, indicating the physical linkage of some immune genes in C. farreri. A cluster of membrane transport genes was also observed; these genes might play important roles in eliminating toxins in C. farreri, which lives as a filter feeder. Further analysis showed 15.43% of the BAC sequence was repetitive. Tandem repeats were the most abundant repeat type, followed by transposable elements. A total of 31 SSRs were predicted in the four BACs. An IS10 family transposon was identified, and a suspected regulatory non-coding RNA gene for this transposon (RNA-OUT) was observed to overlap with it complementarily. This work will promote future studies on the genomics, immune system and non-coding regions of C. farreri.

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Sequencing and analysis of four BAC clones containing innate immune genes from the Zhikong scallop (Chlamys farreri).

http://t.co/lGwpCWRJ Biomimetic Design of Protein Nanomaterials for Hydrophobic Molecular Transport http://t.co/mcnS8tnF

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http://t.co/oyx8wJHr Biomimetic Design of Protein Nanomaterials for Hydrophobic Molecular Transport http://t.co/OoKLxJ3c

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From a purely macromolecular perspective, more protein than lipid in a cell membrane is not necessarily inconsistent with passive transport

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From a purely macromolecular perspective, more protein than lipid in a cell membrane is not necessarily inconsistent with passive transport

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